Реферат: The activity of biocatalysts based on peroxidase enzyme immobilized on Al2O3, SiO2, and Fe3O4 magnetic particles (the use of which is a promising line of biotechnology) is considered. The activity of the biocatalysts is studied in the catalytic oxidation of 2,3,6-trimethylphenol (TMP) to 2,3,5-trimethylhydroquinone (TMHQ), a half-product of vitamin E synthesis. The advantages of using Fe3O4 magnetic particles for peroxidase immobilization in the catalytic synthesis of 2,3,5-trimethylhydroquinone are demonstrated. The optimum conditions for the oxidation of 2,3,6-trimethylphenol are found to be pH 7.2 and 50°C. The method employed for synthesizing Fe3O4 magnetic nanoparticles using inexpensive raw materials and the procedure for the catalytic oxidation of TMP to TMHQ can be recommended as an alternative to the classical industrial method for producing TMHQ.

Библиографическая ссылка: Matveeva O.V. , Lakina N.V. , Doluda V.Y. , Shkileva I.P. , Matveeva V.G. , Sulman E.M.
Effect of peroxidase immobilization on the activity of biocatalysts in trimethylphenol oxidation
Catalysis in Industry. 2015. V.7. N2. P.161-169. DOI: 10.1134/s2070050415020063 WOS Scopus РИНЦ OpenAlex

Оригинальная версия: Матвеева О.В. , Лакина Н.В. , Долуда В.Ю. , Шкилева И.П. , Матвеева В.Г. , Сульман Э.М.
Влияние способа иммобилизации пероксидазы на активность биокатализатора в процессе окисления триметилфенола
Катализ в промышленности. 2015. №1. С.70-78. DOI: 10.18412/1816-0387-2015-1-70-78 РИНЦ CAPlusCAРЖ ВИНИТИ OpenAlex

Даты:

Поступила в редакцию:	4 июн. 2014 г.
Опубликована в печати:	1 апр. 2015 г.
Опубликована online:	25 июн. 2015 г.

Идентификаторы БД:

Web of science:	WOS:000372437200008
Scopus:	2-s2.0-84934946638
РИНЦ:	23984860
OpenAlex:	W844026210

Цитирование в БД:

БД	Цитирований
OpenAlex	2
Web of science	2
Scopus	2

Альметрики: